In the last year, we have applied our method of computationally accounting for surface site heterogeneity to a study of a model protein immobilized with different chemical strategies and on different sensor surfaces. We found that the most uniform surface site distributions were achieved with linker layers of moderate length. We identified experimental conditions that impose increased mass transport limitations. As an additional result of these studies, we have released an updated version of our distributable SPR data anlaysis software. This now also includes a discrete conformational change model, which allows testing of how well the hypothesis of slow conformational changes after an initial binding step fits experimental multi-phasic surface binding data, in comparison with the alternative explanation of surface site distributions with polydisperse affinity and kinetic constants. This was applied to data from the laboratory of Dr. Birgit Helm. Finally, we have continued the collaboration with the laboratory of Dr. Michael Tarlov at NIST on the recognition of different carbohydrate moieties on glycoproteins by surface-immobilized lectins.